A purified thermostable gellan lyase, produced by a thermophilic bacterium, Geobacillus stearothermophilus 98, was characterized in relation to its physicochemical properties. The gellan lyase was established to have a molecular weight of 216 kDa, defined by capillary gel electrophoresis. Amino acid analysis revealed high quantities of Lys, His, Ala, Val, Ile, Glx, and Pro residues. The circular dichroism revealed 45% β-structure and practically lack of α-spiral domains. Kinetic studies showed high affinity of the enzyme to gellan as a substrate (Km = 0.21 μM). The thermal denaturation investigated by cicular dichroism showed a highly cooperative transition with a midpoint (Tm) at about 75 °C. A single product was identified after enzyme action on gellan. Large exothermic aggregation near Tm was observed by differential scanning calorimetry. Two types of gellan lyase crystals were reproducibly isolated.
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Zeitschrift für Naturforschung C
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Physicochemical Characteristics of a Thermostable Gellan Lyase from Geobacillus stearothermophilus 98
Anna Derekova
- Department of Extremophilic Bacteria, Institute of Microbiology, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., bl. 26, Sofi a 1113, Bulgaria. Fax: +3 59 28 70 01 09
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- Department of Extremophilic Bacteria, Institute of Microbiology, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., bl. 26, Sofia 1113, Bulgaria. Fax: +3 59 28 70 01 09
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- Department of Chemistry and Biophysics of Proteins and Enzymes, Institute of Organic Chemistry, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., bl. 9, Sofia 1113, Bulgaria
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- Department of Chemistry and Biophysics of Proteins and Enzymes, Institute of Organic Chemistry, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., bl. 9, Sofia 1113, Bulgaria
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- Department of Protein Biophysics, Institute of Biophysics, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., bl. 21, Sofia 1113, Bulgaria
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- Department of Extremophilic Bacteria, Institute of Microbiology, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., bl. 26, Sofia 1113, Bulgaria. Fax: +3 59 28 70 01 09
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- Dairy Science and Technology Laboratory, Agricultural Research Center of Mabegondo (CIAM), Xunta de Galicia, Carretera de Betan, a Mesón do Vento Km. 8, 15309 Abegondo (Mabegondo), Apdo. 10, 15080 La Coruña, Spain
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- Dairy Science and Technology Laboratory, Agricultural Research Center of Mabegondo (CIAM), Xunta de Galicia, Carretera de Betan, a Mesón do Vento Km. 8, 15309 Abegondo (Mabegondo), Apdo. 10, 15080 La Coruña, Spain
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- Department of Extremophilic Bacteria, Institute of Microbiology, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., bl. 26, Sofia 1113, Bulgaria. Fax: +3 59 28 70 01 09
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Published Online: 2014-06-02 | DOI: https://doi.org/10.1515/znc-2010-3-411
Open Access
Keywords: Thermostable Gellan Lyase; Amino Acid Composition; Crystals
About the article
Received: 2009-11-16
Revised: 2009-12-18
Published Online: 2014-06-02
Published in Print: 2010-04-01
Citation Information: Zeitschrift für Naturforschung C, Volume 65, Issue 3-4, Pages 231–238, ISSN (Online) 1865-7125, ISSN (Print) 0939-5075, DOI: https://doi.org/10.1515/znc-2010-3-411.
© 1946 – 2014: Verlag der Zeitschrift für Naturforschung. This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License. BY-NC-ND 3.0
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- Essential Region for 3-N Methylation in N-Methyltransferases Involved in Caffeine Biosynthesis
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